English to Russian Science Biology (-tech,-chem,micro-)

Amino acids can stabilize proteins by a variety of mechanisms including preferential hydration and direct binding as well as via buffering capacity or antioxidant properties [55,56].The most commonly used amino acids to stabilize proteins as pharmaceutical excipients include histidine, arginine and glycine. Histidine has been used extensively as a buffering agent with proteins such as antibodies [57] and has been shown to not only control solution pH, but to also provide stabilizing non-covalent interactions with antibodies in the solid state [58].
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Arginine is an interesting example of a well-known participant of cation-π interactions [366,368].
As previously mentioned, arginine has been used to increase protein solubility, stability and to dramatically reduce the viscosity of high concentration protein solutions. However, scientists have argued over the mechanistic basis of arginine effects for decades [55,63,314,365,370,371]. In fact, pioneers in this field, Arakawa and Timasheff, have invoked multiple mechanistic hypotheses regarding arginine's unique behavior including surface tension effects, preferential hydration, and preferential interaction [55]. It seems apparent that arginine affects proteins via multiple types of interactions, and likely via multiple mechanisms, as determined by the vast majority of interactions detailed throughout this review (also see Table 3).

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